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Related Experiment Videos

ARF6 controls post-endocytic recycling through its downstream exocyst complex effector.

Magali Prigent1, Thierry Dubois, Graça Raposo

  • 1Membrane and Cytoskeleton Dynamics Group, UMR144 Centre National de la Recherche Scientifique, Institut Curie, 26 rue d'Ulm, F-75248 Paris cedex 05, France.

The Journal of Cell Biology
|December 10, 2003
PubMed
Summary

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ADP-ribosylation factor 6 (ARF6) interacts with the exocyst complex subunit Sec10 to regulate membrane recycling. This interaction is crucial for plasma membrane remodeling and cell spreading during endocytic pathway function.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • ADP-ribosylation factor 6 (ARF6) is a small GTPase regulating membrane dynamics.
  • The exocyst complex is essential for tethering vesicles to the plasma membrane.
  • Membrane recycling via the endocytic pathway is critical for cell function.

Purpose of the Study:

  • To investigate the interaction between ARF6 and the exocyst complex.
  • To elucidate the role of Sec10 in ARF6-mediated membrane recycling.
  • To understand how ARF6 and exocyst components regulate plasma membrane remodeling.

Main Methods:

  • Co-immunoprecipitation to study protein interactions.
  • Immunofluorescence microscopy to analyze protein localization.

Related Experiment Videos

  • Depletion of exocyst subunits (Sec5) and dominant inhibition of Sec10.
  • Analysis of cell morphology and spreading.

    • Main Results:

    • GTP-bound ARF6 directly interacts with Sec10, an exocyst subunit.
    • Sec10 localizes to recycling endosomes and redistributes to plasma membrane ruffling sites upon ARF6 activation.
    • Depletion of Sec5 or inhibition of Sec10 impairs recycling pathway function and ARF6-induced cell spreading.

    Conclusions:

    • ARF6 specifies the delivery and insertion of recycling membranes to dynamic plasma membrane regions.
    • The interaction between ARF6 and the exocyst complex (Sec10) is vital for membrane recycling and cell shape regulation.
    • This study reveals a novel mechanism linking ARF6 signaling to the exocyst machinery for plasma membrane organization.